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Fluorometric Studies of Biologically Important Molecular Complexes

  • Chapter
Modern Fluorescence Spectroscopy

Part of the book series: Modern Analytical Chemistry ((MOAC))

Abstract

Fluorometry has been extensively employed in studies involving molecular complexes because of its exceptional sensitivity and time resolution. Molecular complexation is widespread in nature; indeed, it is through that process that biopolymers such as DNA and enzymes are assembled and carry out their functions. Covalent binding holds together strong complexes, while hydrogen-bonding, charge-transfer, electrostatic, and hydrophobic interactions are mainly responsible for the stability of weaker complexes. Some high-molecular-weight complexes contain fluorescent building blocks that report on their immediate environment; e.g., proteins contain tryptophan and tyrosine fluorescent amino acid residues. Other biomolecules may be labeled with fluorophores by forming noncovalent or covalent complexes. Time-resolved and time-integrated fluorometric investigations of these systems yield information pertaining to the following:

  1. (a)

    the polarity and fluidity of the microenvironment of the emitter,

  2. (b)

    the occurrence of structural fluctuations in the biomolecule within the time span of light emission,

  3. (c)

    the occurrence of excited-state time-dependent interactions between the emitter and the solvent or neighboring chemical groups of the biomolecule,

  4. (d)

    the overall shape and dimensions of the biomolecule,

  5. (e)

    and the exchange of excitation energy between the emitter and other components of the biomolecule.

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Georghiou, S. (1981). Fluorometric Studies of Biologically Important Molecular Complexes. In: Wehry, E.L. (eds) Modern Fluorescence Spectroscopy. Modern Analytical Chemistry. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-1092-1_5

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